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Volumn 97, Issue 14, 2013, Pages 6279-6292

Characterization of recombinant amylopullulanase (gt-apu) and truncated amylopullulanase (gt-apuT) of the extreme thermophile Geobacillus thermoleovorans NP33 and their action in starch saccharification

Author keywords

Amylopullulanase; Geobacillus thermoleovorans; Pullulan; Starch; Truncated amylopullulanase

Indexed keywords

AMYLOPULLULANASE; CATALYTIC EFFICIENCIES; END-PRODUCT ANALYSIS; EXTREME THERMOPHILE; GEOBACILLUS THERMOLEOVORANS; PULLULANS; RECOMBINANT ENZYMES; SUBSTRATE SPECIFICITY;

EID: 84879842967     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-012-4538-6     Document Type: Article
Times cited : (62)

References (67)
  • 1
    • 4143110558 scopus 로고    scopus 로고
    • Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase
    • 10.1016/j.jmb.2004.06.059 1:CAS:528:DC%2BD2cXmsVCrtLk%3D
    • Acharya P, Rajakumara E, Sankaranarayanana R, Rao N (2004) Structural basis of selection and thermostability of laboratory evolved Bacillus subtilis lipase. J Mol Biol 341:1271-1281
    • (2004) J Mol Biol , vol.341 , pp. 1271-1281
    • Acharya, P.1    Rajakumara, E.2    Sankaranarayanana, R.3    Rao, N.4
  • 3
    • 0030908595 scopus 로고    scopus 로고
    • A classification of dextran-hydrolysing enzymes based on amino acid sequence similarities
    • 1:CAS:528:DyaK2sXjtFKjuro%3D
    • Aoki H, Sakano Y (1997) A classification of dextran-hydrolysing enzymes based on amino acid sequence similarities. J Biochem 323:859-861
    • (1997) J Biochem , vol.323 , pp. 859-861
    • Aoki, H.1    Sakano, Y.2
  • 4
    • 85007778637 scopus 로고
    • An alkaline amylopullulanase from alkalophilic Bacillus sp. KSM-1378; Kinetic evidence for two independent active sites for the α- 1,4 and α- 1,6 hydrolytic reactions
    • 10.1271/bbb.59.662 1:CAS:528:DyaK2MXlsVSmtLY%3D
    • Ara K, Igarashi K, Saeki K, Ito S (1995) An alkaline amylopullulanase from alkalophilic Bacillus sp. KSM-1378; kinetic evidence for two independent active sites for the α- 1,4 and α- 1,6 hydrolytic reactions. Biosci Biotechnol Biochem 59:662-665
    • (1995) Biosci Biotechnol Biochem , vol.59 , pp. 662-665
    • Ara, K.1    Igarashi, K.2    Saeki, K.3    Ito, S.4
  • 5
    • 0028904973 scopus 로고
    • Purification and characterization of an alkaline amylopullulanase with both α-1,4 and α-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378
    • 10.1016/0304-4165(94)00148-Q
    • Ara K, Saeki K, Igarashi K, Takaiwa M, Uemura T, Hagihara H, Kawai S, Ito S (1994) Purification and characterization of an alkaline amylopullulanase with both α-1,4 and α-1,6 hydrolytic activity from alkalophilic Bacillus sp. KSM-1378. Biochim Biophys Acta 1243:315-324
    • (1994) Biochim Biophys Acta , vol.1243 , pp. 315-324
    • Ara, K.1    Saeki, K.2    Igarashi, K.3    Takaiwa, M.4    Uemura, T.5    Hagihara, H.6    Kawai, S.7    Ito, S.8
  • 7
    • 33748037939 scopus 로고
    • Amylases, α and β
    • Bernfeld P (1955) Amylases, α and β. Methods Enzymol 1:149-158
    • (1955) Methods Enzymol , vol.1 , pp. 149-158
    • Bernfeld, P.1
  • 8
    • 34748886064 scopus 로고    scopus 로고
    • The 'pair of sugar tongs' site on the non-catalytic domain C of barley-amylase participates in substrate binding and activity
    • 10.1111/j.1742-4658.2007.06024.x 1:CAS:528:DC%2BD2sXhtFeks77K
    • Bozonnet S, Jensen MT, Nielsen MM, Aghajari N, Jensen MH, Kramhoft B, Willemoes M, Tranier S, Haser R, Svensson B (2007) The 'pair of sugar tongs' site on the non-catalytic domain C of barley-amylase participates in substrate binding and activity. FEBS J 274:5055-5067
    • (2007) FEBS J , vol.274 , pp. 5055-5067
    • Bozonnet, S.1    Jensen, M.T.2    Nielsen, M.M.3    Aghajari, N.4    Jensen, M.H.5    Kramhoft, B.6    Willemoes, M.7    Tranier, S.8    Haser, R.9    Svensson, B.10
  • 9
    • 0032989826 scopus 로고    scopus 로고
    • The amylopullulanase of Bacillus sp. DSM 405
    • 10.1007/s002530051378 1:CAS:528:DyaK1MXitVSrurw%3D
    • Brunswick JM, Kelly CT, Fogarty WM (1999) The amylopullulanase of Bacillus sp. DSM 405. Appl Microbiol Biotechnol 51:170-175
    • (1999) Appl Microbiol Biotechnol , vol.51 , pp. 170-175
    • Brunswick, J.M.1    Kelly, C.T.2    Fogarty, W.M.3
  • 10
    • 58149200943 scopus 로고    scopus 로고
    • The carbohydrate-active enzymes database (CAZy): An expert resource for glycogenomics
    • 10.1093/nar/gkn663 10.1093/nar/gkn663 1:CAS:528:DC%2BD1cXhsFejtL7K
    • Cantarel BL, Coutinho PM, Rancurel C, Bernard T, Lombard V, Henrissat B (2009) The carbohydrate-active enzymes database (CAZy): an expert resource for glycogenomics. Nucleic Acids Res 37:D233-D238. doi: 10.1093/nar/gkn663
    • (2009) Nucleic Acids Res , vol.37
    • Cantarel, B.L.1    Coutinho, P.M.2    Rancurel, C.3    Bernard, T.4    Lombard, V.5    Henrissat, B.6
  • 11
    • 0028297041 scopus 로고
    • Chemical modification of xylanase from alkalothermophilic Bacillus species: Evidence for essential carboxyl group
    • 10.1016/0167-4838(94)90004-3 1:CAS:528:DyaK2cXhvVKjtbk%3D
    • Chauthaiwale J, Rao M (1994) Chemical modification of xylanase from alkalothermophilic Bacillus species: evidence for essential carboxyl group. Biochim Biophys Acta 1204:164-168
    • (1994) Biochim Biophys Acta , vol.1204 , pp. 164-168
    • Chauthaiwale, J.1    Rao, M.2
  • 12
    • 0034979496 scopus 로고    scopus 로고
    • Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23
    • 10.1042/BA20010003 1:CAS:528:DC%2BD3MXkslWkurc%3D
    • Chen JT, Chen MC, Chen LL, Chu WS (2001) Structure and expression of an amylopullulanase gene from Bacillus stearothermophilus TS-23. Biotech Appl Bochem 33:189-199
    • (2001) Biotech Appl Bochem , vol.33 , pp. 189-199
    • Chen, J.T.1    Chen, M.C.2    Chen, L.L.3    Chu, W.S.4
  • 13
    • 69449083006 scopus 로고    scopus 로고
    • The carbohydrate-binding module family 20-diversity, structure, and function
    • 10.1111/j.1742-4658.2009.07221.x 1:CAS:528:DC%2BD1MXhtFChtrjN
    • Christiansen C, Abou Hachem M, Janecek S, Vikso-Nielsen A, Blennow A, Svensson B (2009) The carbohydrate-binding module family 20-diversity, structure, and function. FEBS J 276:5006-5029
    • (2009) FEBS J , vol.276 , pp. 5006-5029
    • Christiansen, C.1    Abou Hachem, M.2    Janecek, S.3    Vikso-Nielsen, A.4    Blennow, A.5    Svensson, B.6
  • 14
    • 0023413269 scopus 로고
    • Cloning of the debranching-enzyme gene from Thermoanaerobium brockii into Escherichia coli and Bacillus subtilis
    • 1:CAS:528:DyaL2sXlsVymtL0%3D
    • Coleman RD, Yang SS, McAlister MP (1987) Cloning of the debranching-enzyme gene from Thermoanaerobium brockii into Escherichia coli and Bacillus subtilis. J Bacteriol 169:4302-4307
    • (1987) J Bacteriol , vol.169 , pp. 4302-4307
    • Coleman, R.D.1    Yang, S.S.2    McAlister, M.P.3
  • 15
    • 0036238532 scopus 로고    scopus 로고
    • Purification and characterization of maltooligosaccharide-forming amylase from Bacillus circulans GRS 313
    • 10.1038/sj.jim.7000220 1:CAS:528:DC%2BD38XivVeqtrs%3D
    • Dey G, Palit S, Banerjee R, Maiti BR (2002) Purification and characterization of maltooligosaccharide-forming amylase from Bacillus circulans GRS 313. J Ind Microbiol Biotechnol 28:193-200
    • (2002) J Ind Microbiol Biotechnol , vol.28 , pp. 193-200
    • Dey, G.1    Palit, S.2    Banerjee, R.3    Maiti, B.R.4
  • 16
    • 0033760418 scopus 로고    scopus 로고
    • A new thermoactive pullulanase from Desulfurococcus mucosus: Cloning, sequencing, purification, and characterization of the recombinant enzyme after expression in Bacillus subtilis
    • 10.1128/JB.182.22.6331-6338.2000 1:CAS:528:DC%2BD3cXnvVGhurs%3D
    • Duffner F, Bertoldo C, Andersen JT, Wagner K, Antranikian G (2000) A new thermoactive pullulanase from Desulfurococcus mucosus: cloning, sequencing, purification, and characterization of the recombinant enzyme after expression in Bacillus subtilis. J Bacteriol 182:6331-6338
    • (2000) J Bacteriol , vol.182 , pp. 6331-6338
    • Duffner, F.1    Bertoldo, C.2    Andersen, J.T.3    Wagner, K.4    Antranikian, G.5
  • 17
    • 0001634232 scopus 로고
    • Thin layer chromatographic method for identification of oligosaccharides in starch hydrolysates
    • 10.1016/S0021-9673(01)82270-6 1:CAS:528:DyaE2MXhtlGis70%3D
    • Hansen SA (1975) Thin layer chromatographic method for identification of oligosaccharides in starch hydrolysates. J Chromatogr 105:388-390
    • (1975) J Chromatogr , vol.105 , pp. 388-390
    • Hansen, S.A.1
  • 18
    • 0029661443 scopus 로고    scopus 로고
    • Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites
    • 10.1074/jbc.271.39.24075 1:CAS:528:DyaK28XlvFSqt7g%3D
    • Hatada Y, Igarashi K, Ozaki K, Ara K, Hitomi J, Kobayashi T, Kawai S, Watabe T, Ito S (1996) Amino acid sequence and molecular structure of an alkaline amylopullulanase from Bacillus that hydrolyzes α-1,4 and α-1,6 linkages in polysaccharides at different active sites. J Biol Chem 271:24075-24083
    • (1996) J Biol Chem , vol.271 , pp. 24075-24083
    • Hatada, Y.1    Igarashi, K.2    Ozaki, K.3    Ara, K.4    Hitomi, J.5    Kobayashi, T.6    Kawai, S.7    Watabe, T.8    Ito, S.9
  • 19
    • 0013893901 scopus 로고
    • Kinetic studies on glucoamylase II. competition between two types of substrate having α-1,4 and α-1,6 glucosidic linkage
    • 1:CAS:528:DyaF28XktFeltbc%3D
    • Hiromi K, Hamauzu Z-I, Takahashi K, Ono S (1966) Kinetic studies on glucoamylase II. competition between two types of substrate having α-1,4 and α-1,6 glucosidic linkage. J Biochem 59:411-418
    • (1966) J Biochem , vol.59 , pp. 411-418
    • Hiromi, K.1    Hamauzu, Z.-I.2    Takahashi, K.3    Ono, S.4
  • 20
    • 0012286188 scopus 로고    scopus 로고
    • How many conserved sequence regions are there in the α-amylase family?
    • 1:CAS:528:DC%2BD3sXhtVClurc%3D
    • Janecek S (2002) How many conserved sequence regions are there in the α-amylase family? Biologia 57(suppl 11):29-41
    • (2002) Biologia , vol.57 , Issue.SUPPL. 11 , pp. 29-41
    • Janecek, S.1
  • 21
    • 33748670795 scopus 로고    scopus 로고
    • Amylolytic families of glycoside hydrolases: Focus on the family GH-57
    • 1:CAS:528:DC%2BD28XhvVCrt7c%3D
    • Janecek S (2005) Amylolytic families of glycoside hydrolases: focus on the family GH-57. Biologia 60(suppl 16):177-184
    • (2005) Biologia , vol.60 , Issue.SUPPL. 16 , pp. 177-184
    • Janecek, S.1
  • 22
    • 80054683038 scopus 로고    scopus 로고
    • Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals
    • 10.1016/j.enzmictec.2011.07.002 1:CAS:528:DC%2BC3MXhtlejsr3M
    • Janecek S, Svensson B, MacGregor EA (2011) Structural and evolutionary aspects of two families of non-catalytic domains present in starch and glycogen binding proteins from microbes, plants and animals. Enz Microb Technol 49:429-440
    • (2011) Enz Microb Technol , vol.49 , pp. 429-440
    • Janecek, S.1    Svensson, B.2    Macgregor, E.A.3
  • 23
    • 79955975196 scopus 로고    scopus 로고
    • Structural and functional analysis of GH57 family thermostable amylopullulanase
    • 1:CAS:528:DC%2BC3MXisFSgsbg%3D
    • Jiao Y, Wang S, Lv M (2011) Structural and functional analysis of GH57 family thermostable amylopullulanase. Wei Sheng Wu Xue Bao 51:21-28
    • (2011) Wei Sheng Wu Xue Bao , vol.51 , pp. 21-28
    • Jiao, Y.1    Wang, S.2    Lv, M.3
  • 24
    • 0028814170 scopus 로고
    • Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide
    • 10.1111/j.1432-1033.1995.tb20189.x 1:CAS:528:DyaK2MXktV2msLw%3D
    • Kim C-H, Kim YS (1995) Substrate specificity and detailed characterization of a bifunctional amylase-pullulanase enzyme from Bacillus circulans F-2 having two different active sites on one polypeptide. Eur J Biochem 227:687-693
    • (1995) Eur J Biochem , vol.227 , pp. 687-693
    • Kim, C.-H.1    Kim, Y.S.2
  • 25
    • 57849098719 scopus 로고    scopus 로고
    • Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137
    • 10.1263/jbb.106.449 1:CAS:528:DC%2BD1MXhvVymsrg%3D
    • Kim JH, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M (2008) Characterization of gene encoding amylopullulanase from plant-originated lactic acid bacterium, Lactobacillus plantarum L137. J Biosci Bioeng 106:449-459
    • (2008) J Biosci Bioeng , vol.106 , pp. 449-459
    • Kim, J.H.1    Sunako, M.2    Ono, H.3    Murooka, Y.4    Fukusaki, E.5    Yamashita, M.6
  • 26
    • 60949105812 scopus 로고    scopus 로고
    • Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137
    • 10.1016/j.jbiosc.2008.10.019 1:CAS:528:DC%2BD1MXkvFGltrc%3D
    • Kim JH, Sunako M, Ono H, Murooka Y, Fukusaki E, Yamashita M (2009) Characterization of the C-terminal truncated form of amylopullulanase from Lactobacillus plantarum L137. J Biosci Bioeng 107:124-129
    • (2009) J Biosci Bioeng , vol.107 , pp. 124-129
    • Kim, J.H.1    Sunako, M.2    Ono, H.3    Murooka, Y.4    Fukusaki, E.5    Yamashita, M.6
  • 27
    • 0032942009 scopus 로고    scopus 로고
    • Modes of the action of acarbose hydrolysis and transglycolysation catalysed by a thermostable maltogenic amylase, the gene of which was cloned from a Thermus strain
    • Kim TJ, Kim MJ, Kim BC, Kim JC, Cheong TK, Kim JW (1999) Modes of the action of acarbose hydrolysis and transglycolysation catalysed by a thermostable maltogenic amylase, the gene of which was cloned from a Thermus strain. Appl Env Microbiol 56:1644-1651
    • (1999) Appl Env Microbiol , vol.56 , pp. 1644-1651
    • Kim, T.J.1    Kim, M.J.2    Kim, B.C.3    Kim, J.C.4    Cheong, T.K.5    Kim, J.W.6
  • 28
    • 0028967090 scopus 로고
    • Complete inactivation of Escherichia coli uridine phosphorylase by modification of asp with Woodwards reagent k
    • 10.1074/jbc.270.17.10050 1:CAS:528:DyaK2MXltlWns7w%3D
    • Komissarov AA, Romanova DV, Debabov VG (1995) Complete inactivation of Escherichia coli uridine phosphorylase by modification of asp with Woodwards reagent k. J Biol Chem 270:10050-10055
    • (1995) J Biol Chem , vol.270 , pp. 10050-10055
    • Komissarov, A.A.1    Romanova, D.V.2    Debabov, V.G.3
  • 29
    • 0032976301 scopus 로고    scopus 로고
    • The concept of the α-amylase family: Structural similarity and common catalytic mechanism
    • 10.1016/S1389-1723(99)80114-5 1:CAS:528:DyaK1MXltFCmu74%3D
    • Kuriki T, Imanaka T (1999) The concept of the α-amylase family: structural similarity and common catalytic mechanism. J Biosci Bioeng 87:557-565
    • (1999) J Biosci Bioeng , vol.87 , pp. 557-565
    • Kuriki, T.1    Imanaka, T.2
  • 30
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • 10.1038/227680a0 1:CAS:528:DC%2BD3MXlsFags7s%3D
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 31
    • 0028146782 scopus 로고
    • Gene cloning and characterization of α-amylase-pullulanase (AapT) from thermophilic and alkaliphilic Bacillus sp. XAL601
    • 1:CAS:528:DyaK2MXhtFahu74%3D
    • Lee S-P, Morikawa M, Takagi M, Imanaka T (1994) Gene cloning and characterization of α-amylase-pullulanase (AapT) from thermophilic and alkaliphilic Bacillus sp. XAL601. Appl Env Microbiol 60:3764-3773
    • (1994) Appl Env Microbiol , vol.60 , pp. 3764-3773
    • Lee, S.-P.1    Morikawa, M.2    Takagi, M.3    Imanaka, T.4
  • 32
    • 50649108593 scopus 로고    scopus 로고
    • Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues
    • 10.1007/s00792-008-0168-4 1:CAS:528:DC%2BD1cXhtVekt7bM
    • Lin HY, Chuang HH, Lin FP (2008) Biochemical characterization of engineered amylopullulanase from Thermoanaerobacter ethanolicus 39E-implicating the non-necessity of its 100 C-terminal amino acid residues. Extremophiles 12:641-650
    • (2008) Extremophiles , vol.12 , pp. 641-650
    • Lin, H.Y.1    Chuang, H.H.2    Lin, F.P.3
  • 33
    • 0036183142 scopus 로고    scopus 로고
    • Cloning, expression, and characterization of thermostable region of amylopullulanase gene from Thermoanaerobacter ethanolicus 39E
    • 10.1385/ABAB:97:1:33 1:CAS:528:DC%2BD38XitFynsrg%3D
    • Lin FP, Leu KL (2002) Cloning, expression, and characterization of thermostable region of amylopullulanase gene from Thermoanaerobacter ethanolicus 39E. Appl Biochem Biotechnol 97:33-44
    • (2002) Appl Biochem Biotechnol , vol.97 , pp. 33-44
    • Lin, F.P.1    Leu, K.L.2
  • 34
    • 81355147636 scopus 로고    scopus 로고
    • Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region
    • 10.1007/s12010-011-9319-7 1:CAS:528:DC%2BC3MXhsVars7rO
    • Lin FP, Ma HY, Lin HJ, Liu SM, Tzou WS (2011) Biochemical characterization of two truncated forms of amylopullulanase from Thermoanaerobacterium saccharolyticum NTOU1 to identify its enzymatically active region. Appl Biochem Biotechnol 165:1047-1056
    • (2011) Appl Biochem Biotechnol , vol.165 , pp. 1047-1056
    • Lin, F.P.1    Ma, H.Y.2    Lin, H.J.3    Liu, S.M.4    Tzou, W.S.5
  • 35
    • 77952891256 scopus 로고    scopus 로고
    • Gene cloning, overexpression, and characterization of a xylanase from Penicillium sp. CGMCC 1699
    • 10.1007/s12010-009-8719-4 1:CAS:528:DC%2BC3cXlsVaitLY%3D
    • Liu W, Shi P, Chen Q, Yang P, Wang G, Wang Y, Luo H, Yao B (2010) Gene cloning, overexpression, and characterization of a xylanase from Penicillium sp. CGMCC 1699. Appl Biochem Biotechnol 162:1-12
    • (2010) Appl Biochem Biotechnol , vol.162 , pp. 1-12
    • Liu, W.1    Shi, P.2    Chen, Q.3    Yang, P.4    Wang, G.5    Wang, Y.6    Luo, H.7    Yao, B.8
  • 36
    • 71849104860 scopus 로고
    • Protein measurement with the folin phenol reagent
    • 1:CAS:528:DyaG38XhsVyrsw%3D%3D
    • Lowry OH, Rosebrough NJ, Farr AL, Randall RJ (1951) Protein measurement with the folin phenol reagent. J Biol Chem 193:265-275
    • (1951) J Biol Chem , vol.193 , pp. 265-275
    • Lowry, O.H.1    Rosebrough, N.J.2    Farr, A.L.3    Randall, R.J.4
  • 37
    • 0035831255 scopus 로고    scopus 로고
    • Relationship of sequence and structure to specificity in the α-amylase family of enzymes
    • 10.1016/S0167-4838(00)00302-2 1:CAS:528:DC%2BD3MXhvVagtLk%3D
    • MacGregor EA, Janecek S, Svensson B (2001) Relationship of sequence and structure to specificity in the α-amylase family of enzymes. Biochim Biophys Acta 1546:1-20
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 1-20
    • Macgregor, E.A.1    Janecek, S.2    Svensson, B.3
  • 38
    • 0027257462 scopus 로고
    • Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis
    • 1:CAS:528:DyaK3sXmt1Sguro%3D
    • Mathupala SP, Lowe SE, Podkovyrov SM, Zeikus JG (1993) Sequencing of the amylopullulanase (apu) gene of Thermoanaerobacter ethanolicus 39E, and identification of the active site by site-directed mutagenesis. J Biol Chem 268:16332-16344
    • (1993) J Biol Chem , vol.268 , pp. 16332-16344
    • Mathupala, S.P.1    Lowe, S.E.2    Podkovyrov, S.M.3    Zeikus, J.G.4
  • 39
    • 0025012804 scopus 로고
    • Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum
    • 10.1016/0006-291X(90)91920-N 1:CAS:528:DyaK3cXhtFCksr0%3D
    • Mathupala S, Saha BC, Zeikus JG (1990) Substrate competition and specificity at the active site of amylopullulanase from Clostridium thermohydrosulfuricum. Biochem Biophys Res Commun 166:126-132
    • (1990) Biochem Biophys Res Commun , vol.166 , pp. 126-132
    • Mathupala, S.1    Saha, B.C.2    Zeikus, J.G.3
  • 40
    • 0021395910 scopus 로고
    • Structure and possible catalytic residues of Taka amylase A
    • 1:CAS:528:DyaL2cXhsFejtbo%3D
    • Matsuura Y, Kusunoki M, Harada W, Kakudo M (1984) Structure and possible catalytic residues of Taka amylase A. J Biochem 95:697-702
    • (1984) J Biochem , vol.95 , pp. 697-702
    • Matsuura, Y.1    Kusunoki, M.2    Harada, W.3    Kakudo, M.4
  • 41
    • 0024287178 scopus 로고
    • Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulfuricum
    • 1:CAS:528:DyaL1cXhs1ekurs%3D
    • Melasniemi H (1988) Purification and some properties of the extracellular α-amylase-pullulanase produced by Clostridium thermohydrosulfuricum. J Biochem 250:813-818
    • (1988) J Biochem , vol.250 , pp. 813-818
    • Melasniemi, H.1
  • 42
    • 0025278162 scopus 로고
    • Nucleotide sequence of α-amylase-pullulanase gene from Clostridium thermohydrosulfuricum
    • 10.1099/00221287-136-3-447 1:CAS:528:DyaK3cXls1Kiu7w%3D
    • Melasniemi H, Paloheimo M, Hemio L (1990) Nucleotide sequence of α-amylase-pullulanase gene from Clostridium thermohydrosulfuricum. J Gen Microbiol 136:447-454
    • (1990) J Gen Microbiol , vol.136 , pp. 447-454
    • Melasniemi, H.1    Paloheimo, M.2    Hemio, L.3
  • 43
    • 33747333106 scopus 로고
    • Use of dinitrosalicylic acid reagent for determination of reducing sugar
    • 10.1021/ac60147a030 1:CAS:528:DyaG1MXmtFKiuw%3D%3D
    • Miller GL (1959) Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal Chem 31:426-428
    • (1959) Anal Chem , vol.31 , pp. 426-428
    • Miller, G.L.1
  • 44
    • 0001051874 scopus 로고    scopus 로고
    • Amylases of the thermophilic fungus Thermomyces lanuginosus; Their purification, properties, action on starch and response to heat
    • 10.1007/BF02703143 1:CAS:528:DyaK2sXitlGgsw%3D%3D
    • Mishra R, Maheshwari R (1996) Amylases of the thermophilic fungus Thermomyces lanuginosus; their purification, properties, action on starch and response to heat. J Biosci 21:653-672
    • (1996) J Biosci , vol.21 , pp. 653-672
    • Mishra, R.1    Maheshwari, R.2
  • 45
    • 33748447483 scopus 로고    scopus 로고
    • 2+ independent amylopullulanase by an extreme thermophile Geobacillus thermoleovorans in submerged fermentation
    • 2+ independent amylopullulanase by an extreme thermophile Geobacillus thermoleovorans in submerged fermentation. Indian J Biotech 5:337-345
    • (2006) Indian J Biotech , vol.5 , pp. 337-345
    • Noorvez, S.M.1    Ezhilvannan, M.2    Satyanarayana, T.3
  • 50
    • 0028038927 scopus 로고
    • Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli
    • 1:CAS:528:DyaK2cXht1KmsL0%3D
    • Ramesh MV, Podkovyrov SM, Lowe SE, Zeikus JG (1994) Cloning and sequencing of the Thermoanaerobacterium saccharolyticum B6A-RI apu gene and purification and characterization of the amylopullulanase from Escherichia coli. Appl Env Microbiol 60:94-101
    • (1994) Appl Env Microbiol , vol.60 , pp. 94-101
    • Ramesh, M.V.1    Podkovyrov, S.M.2    Lowe, S.E.3    Zeikus, J.G.4
  • 51
    • 0028859745 scopus 로고
    • Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli
    • 1:STN:280:DyaK28%2FjtFGksA%3D%3D
    • Rudiger A, Jorgensen PL, Antranikian G (1995) Isolation and characterization of a heat-stable pullulanase from the hyperthermophilic archaeon Pyrococcus woesei after cloning and expression of its gene in Escherichia coli. Appl Env Microbiol 61:567-575
    • (1995) Appl Env Microbiol , vol.61 , pp. 567-575
    • Rudiger, A.1    Jorgensen, P.L.2    Antranikian, G.3
  • 52
    • 0025246656 scopus 로고
    • Characterization of an endo-acting amylopullulanase from Thermoanaerobacter strain B6A
    • 1:CAS:528:DyaK3cXitlWlurg%3D
    • Saha BC, Lamed R, Lee C-Y, Mathupala SP, Zeikus JG (1990) Characterization of an endo-acting amylopullulanase from Thermoanaerobacter strain B6A. Appl Env Microbiol 56:881-886
    • (1990) Appl Env Microbiol , vol.56 , pp. 881-886
    • Saha, B.C.1    Lamed, R.2    Lee, C.-Y.3    Mathupala, S.P.4    Zeikus, J.G.5
  • 53
    • 0024764113 scopus 로고
    • New thermostable α-amylase like pullulanase from thermophilic Bacillus sp. 3183
    • 10.1016/0141-0229(89)90126-9 1:CAS:528:DyaK3cXpsVeitQ%3D%3D
    • Saha BC, Shen GJ, Srivastava KC, LeCureux LW, Zeikus JG (1989) New thermostable α-amylase like pullulanase from thermophilic Bacillus sp. 3183. Enzyme Microb Technol 11:760-764
    • (1989) Enzyme Microb Technol , vol.11 , pp. 760-764
    • Saha, B.C.1    Shen, G.J.2    Srivastava, K.C.3    Lecureux, L.W.4    Zeikus, J.G.5
  • 54
    • 0024722550 scopus 로고
    • Novel highly thermostable pullulanase from thermophiles
    • 10.1016/0167-7799(89)90013-9 1:CAS:528:DyaL1MXlvV2qtr8%3D
    • Saha BC, Zeikus JG (1989) Novel highly thermostable pullulanase from thermophiles. Trends Biotechnol 7:234-239
    • (1989) Trends Biotechnol , vol.7 , pp. 234-239
    • Saha, B.C.1    Zeikus, J.G.2
  • 55
    • 45149146955 scopus 로고
    • Amylase-pullulanase enzyme by B. circulans F-2
    • 10.1016/0304-4165(89)90062-7 1:CAS:528:DyaL1MXkslemtbY%3D
    • Sata H, Umeda M, Kim C, Taniguchi H, Maruyama Y (1989) Amylase-pullulanase enzyme by B. circulans F-2. Biochem Biophys Acta 991:388-394
    • (1989) Biochem Biophys Acta , vol.991 , pp. 388-394
    • Sata, H.1    Umeda, M.2    Kim, C.3    Taniguchi, H.4    Maruyama, Y.5
  • 56
    • 2342584768 scopus 로고    scopus 로고
    • Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles
    • 10.1042/BST0320276 1:CAS:528:DC%2BD2cXjtVSgtbc%3D
    • Satyanarayana T, Noorwez SM, Kumar S, Rao JL, Ezhilvannan M, Kaur P (2004) Development of an ideal starch saccharification process using amylolytic enzymes from thermophiles. Biochem Soc Trans 32:276-278
    • (2004) Biochem Soc Trans , vol.32 , pp. 276-278
    • Satyanarayana, T.1    Noorwez, S.M.2    Kumar, S.3    Rao, J.L.4    Ezhilvannan, M.5    Kaur, P.6
  • 57
    • 1842478437 scopus 로고    scopus 로고
    • Cloning and expression of mycobacterial glutamine synthetase gene in Escherichia coli
    • 10.1016/j.bbrc.2004.03.094 1:CAS:528:DC%2BD2cXivVCru7w%3D
    • Singh J, Joshi MC, Bhatnagar R (2004) Cloning and expression of mycobacterial glutamine synthetase gene in Escherichia coli. Biochem Biophys Res Commun 317:634-638
    • (2004) Biochem Biophys Res Commun , vol.317 , pp. 634-638
    • Singh, J.1    Joshi, M.C.2    Bhatnagar, R.3
  • 58
    • 0033013902 scopus 로고    scopus 로고
    • The starch-binding domain from glucoamylase disrupts the structure of starch
    • 10.1016/S0014-5793(99)00263-X 1:CAS:528:DyaK1MXhvVClsr0%3D
    • Southall SM, Simpson PJ, Gilbert HJ, Williamson G, Williamson MP (1999) The starch-binding domain from glucoamylase disrupts the structure of starch. FEBS Lett 447:58-60
    • (1999) FEBS Lett , vol.447 , pp. 58-60
    • Southall, S.M.1    Simpson, P.J.2    Gilbert, H.J.3    Williamson, G.4    Williamson, M.P.5
  • 59
    • 33845665889 scopus 로고    scopus 로고
    • Dividing the large glycoside hydrolase family 13 into subfamilies: Towards improved functional annotations of α-amylase-related proteins
    • 10.1093/protein/gzl044 1:CAS:528:DC%2BD28Xht1Ohu7rJ
    • Stam MR, Danchin EG, Rancurel C, Coutinho PM, Henrissat B (2006) Dividing the large glycoside hydrolase family 13 into subfamilies: towards improved functional annotations of α-amylase-related proteins. Protein Eng Des Sel 19:555-562
    • (2006) Protein Eng des Sel , vol.19 , pp. 555-562
    • Stam, M.R.1    Danchin, E.G.2    Rancurel, C.3    Coutinho, P.M.4    Henrissat, B.5
  • 60
    • 33644990621 scopus 로고    scopus 로고
    • Sources, properties and suitability of new thermostable enzymes in food processing
    • 10.1080/10408690590957296 1:CAS:528:DC%2BD28Xit1ans7g%3D
    • Synowiecki J, Grzybowska B, Zdzieblo A (2006) Sources, properties and suitability of new thermostable enzymes in food processing. Rit Rev Food Sci Nutrit 46:197-205
    • (2006) Rit Rev Food Sci Nutrit , vol.46 , pp. 197-205
    • Synowiecki, J.1    Grzybowska, B.2    Zdzieblo, A.3
  • 61
    • 0001484876 scopus 로고
    • Pullulanase-amylase complex enzyme from Bacillus subtilis
    • 10.1271/bbb1961.51.9 1:CAS:528:DyaL2sXhslWltLg%3D
    • Takasaki Y (1987) Pullulanase-amylase complex enzyme from Bacillus subtilis. Agric Biol Chem 51:9-16
    • (1987) Agric Biol Chem , vol.51 , pp. 9-16
    • Takasaki, Y.1
  • 62
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0
    • 10.1093/molbev/msm092 1:CAS:528:DC%2BD2sXpsVGrsL8%3D
    • Tamura K, Dudley J, Nei M, Kumar S (2007) MEGA4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24:1596-1599
    • (2007) Mol Biol Evol , vol.24 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 63
    • 35048826310 scopus 로고    scopus 로고
    • Purification and characterization of a hyperthermostable and high maltogenic α-amylase of an extreme thermophile Geobacillus thermoleovorans
    • 10.1007/s12010-007-0017-4
    • Uma Maheshwar Rao JL, Satyanarayana T (2007) Purification and characterization of a hyperthermostable and high maltogenic α-amylase of an extreme thermophile Geobacillus thermoleovorans. Appl Biochem Biotechnol 142:179-193
    • (2007) Appl Biochem Biotechnol , vol.142 , pp. 179-193
    • Uma Maheshwar Rao, J.L.1    Satyanarayana, T.2
  • 64
    • 0029893110 scopus 로고    scopus 로고
    • Thermozymes: Identifying molecular determinant of protein structural and functional stability
    • 10.1016/0167-7799(96)10026-3 1:CAS:528:DyaK28XjsVWitrw%3D
    • Vieille C, Zeikus JG (1996) Thermozymes: identifying molecular determinant of protein structural and functional stability. Tibtech 14(6):183-189
    • (1996) Tibtech , vol.14 , Issue.6 , pp. 183-189
    • Vieille, C.1    Zeikus, J.G.2
  • 65
    • 0035098779 scopus 로고    scopus 로고
    • Hyperthermopilic enzymes: Source, uses, and molecular mechanism for thermostability
    • 10.1128/MMBR.65.1.1-43.2001 1:CAS:528:DC%2BD3MXisFyms74%3D
    • Vieille C, Zeikus JG (2001) Hyperthermopilic enzymes: source, uses, and molecular mechanism for thermostability. Microbiol Mol Biol Rev 65:1-43
    • (2001) Microbiol Mol Biol Rev , vol.65 , pp. 1-43
    • Vieille, C.1    Zeikus, J.G.2
  • 66
    • 28844470263 scopus 로고    scopus 로고
    • Amylopullulanase - A novel enzyme of L. amylophilus GV6 in direct fermentation of starch to L(+) lactic acid
    • 10.1016/j.enzmictec.2005.07.010 1:CAS:528:DC%2BD2MXhtlagsrbF
    • Vishnu C, Naveena B, Md J, Altaf. Venkateshwar M, Gopal R (2006) Amylopullulanase - a novel enzyme of L. amylophilus GV6 in direct fermentation of starch to L(+) lactic acid. Enz Microb Technol 38:545-550
    • (2006) Enz Microb Technol , vol.38 , pp. 545-550
    • Vishnu, C.1    Naveena, B.2    Md, J.3    Altaf. Venkateshwar, M.4    Gopal, R.5
  • 67
    • 33846845195 scopus 로고    scopus 로고
    • Molecular cloning and heterologous expression of a new xylanase gene from Plectosphaerella cucumerina
    • 10.1007/s00253-006-0648-3 1:CAS:528:DC%2BD2sXht1yhurw%3D
    • Zhang GM, Huang J, Huang GR, Ma LX, Zhang XE (2007) Molecular cloning and heterologous expression of a new xylanase gene from Plectosphaerella cucumerina. Appl Microbiol Biotechnol 74:339-346
    • (2007) Appl Microbiol Biotechnol , vol.74 , pp. 339-346
    • Zhang, G.M.1    Huang, J.2    Huang, G.R.3    Ma, L.X.4    Zhang, X.E.5


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